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Conserved domains on  [gi|1958680058|ref|XP_038949240|]
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centromere protein J isoform X1 [Rattus norvegicus]

Protein Classification

T-complex 10 C-terminal domain-containing protein( domain architecture ID 10537651)

T-complex 10 C-terminal domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Tcp10_C pfam07202
T-complex protein 10 C-terminus; This entry represents a repeating unit commonly found in the ...
 1158-1186 4.99e-11

T-complex protein 10 C-terminus; This entry represents a repeating unit commonly found in the C terminus of the eukaryotic T-complex protein 10. The T-complex is involved in spermatogenesis in mice. The repeating unit is commonly found 3-4 times, but there is often a gap between the first and second repeats, which is big enough to accommodate another repeat unit. However, the score is insufficient to be included, and could be a degenerate repeat.


:

Pssm-ID: 462118  Cd Length: 30  Bit Score: 58.21  E-value: 4.99e-11
                           10        20
                   ....*....|....*....|....*....
gi 1958680058 1158 EINHPDGKVEKVYKNGCRVVLFPNGTRKE 1186
Cdd:pfam07202    2 EIIFPDGTVERVYSDGDKVIEFPNGTREI 30
Tcp10_C pfam07202
T-complex protein 10 C-terminus; This entry represents a repeating unit commonly found in the ...
 1267-1295 5.58e-10

T-complex protein 10 C-terminus; This entry represents a repeating unit commonly found in the C terminus of the eukaryotic T-complex protein 10. The T-complex is involved in spermatogenesis in mice. The repeating unit is commonly found 3-4 times, but there is often a gap between the first and second repeats, which is big enough to accommodate another repeat unit. However, the score is insufficient to be included, and could be a degenerate repeat.


:

Pssm-ID: 462118  Cd Length: 30  Bit Score: 55.52  E-value: 5.58e-10
                           10        20
                   ....*....|....*....|....*....
gi 1958680058 1267 EESIFPDGTIVRVQRDGNKIIEFNNGQRE 1295
Cdd:pfam07202    1 EEIIFPDGTVERVYSDGDKVIEFPNGTRE 29
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 905-1140 9.97e-09

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


The actual alignment was detected with superfamily member TIGR02169:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1164  Bit Score: 60.08  E-value: 9.97e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  905 LREKVIELESEIEKFKAENTSLAKLRIERESALEKLRKEIADFEQQKARElaRIEEyKKEETRKLQKERKVFEKYTAA-- 982
Cdd:TIGR02169  742 LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHS--RIPE-IQAELSKLEEEVSRIEARLREie 818

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  983 ----ARTFPDKKEREEIQALKQQIQELQEDLKRKETKWSSTHGRLR---SQIEMLVKENTDLREEIKVMERFRLEAWKRA 1055
Cdd:TIGR02169  819 qklnRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEeleEELEELEAALRDLESRLGDLKKERDELEAQL 898

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058 1056 EAIENspkacqyimatkKDESMNSSIQFQKSHASLGVQGEKYKKKYLPAQGNSSRRSKSVPPRDLgSLDKGQAALPR--- 1132
Cdd:TIGR02169  899 RELER------------KIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEEL-SLEDVQAELQRvee 965

                          250
                   ....*....|
gi 1958680058 1133 --EPLQPVNF 1140
Cdd:TIGR02169  966 eiRALEPVNM 975
Tcp10_C pfam07202
T-complex protein 10 C-terminus; This entry represents a repeating unit commonly found in the ...
 1231-1259 3.88e-05

T-complex protein 10 C-terminus; This entry represents a repeating unit commonly found in the C terminus of the eukaryotic T-complex protein 10. The T-complex is involved in spermatogenesis in mice. The repeating unit is commonly found 3-4 times, but there is often a gap between the first and second repeats, which is big enough to accommodate another repeat unit. However, the score is insufficient to be included, and could be a degenerate repeat.


:

Pssm-ID: 462118  Cd Length: 30  Bit Score: 41.65  E-value: 3.88e-05
                           10        20
                   ....*....|....*....|....*....
gi 1958680058 1231 EVLHFSSGQIEKHFPDGRKEITFPDQTIK 1259
Cdd:pfam07202    1 EEIIFPDGTVERVYSDGDKVIEFPNGTRE 29
Tcp10_C pfam07202
T-complex protein 10 C-terminus; This entry represents a repeating unit commonly found in the ...
 1302-1331 9.57e-05

T-complex protein 10 C-terminus; This entry represents a repeating unit commonly found in the C terminus of the eukaryotic T-complex protein 10. The T-complex is involved in spermatogenesis in mice. The repeating unit is commonly found 3-4 times, but there is often a gap between the first and second repeats, which is big enough to accommodate another repeat unit. However, the score is insufficient to be included, and could be a degenerate repeat.


:

Pssm-ID: 462118  Cd Length: 30  Bit Score: 40.49  E-value: 9.57e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 1958680058 1302 KRREYPDGTVKTVYANGHQETKYTSGRVRV 1331
Cdd:pfam07202    1 EEIIFPDGTVERVYSDGDKVIEFPNGTREI 30
 
Name Accession Description Interval E-value
Tcp10_C pfam07202
T-complex protein 10 C-terminus; This entry represents a repeating unit commonly found in the ...
 1158-1186 4.99e-11

T-complex protein 10 C-terminus; This entry represents a repeating unit commonly found in the C terminus of the eukaryotic T-complex protein 10. The T-complex is involved in spermatogenesis in mice. The repeating unit is commonly found 3-4 times, but there is often a gap between the first and second repeats, which is big enough to accommodate another repeat unit. However, the score is insufficient to be included, and could be a degenerate repeat.


Pssm-ID: 462118  Cd Length: 30  Bit Score: 58.21  E-value: 4.99e-11
                           10        20
                   ....*....|....*....|....*....
gi 1958680058 1158 EINHPDGKVEKVYKNGCRVVLFPNGTRKE 1186
Cdd:pfam07202    2 EIIFPDGTVERVYSDGDKVIEFPNGTREI 30
Tcp10_C pfam07202
T-complex protein 10 C-terminus; This entry represents a repeating unit commonly found in the ...
 1267-1295 5.58e-10

T-complex protein 10 C-terminus; This entry represents a repeating unit commonly found in the C terminus of the eukaryotic T-complex protein 10. The T-complex is involved in spermatogenesis in mice. The repeating unit is commonly found 3-4 times, but there is often a gap between the first and second repeats, which is big enough to accommodate another repeat unit. However, the score is insufficient to be included, and could be a degenerate repeat.


Pssm-ID: 462118  Cd Length: 30  Bit Score: 55.52  E-value: 5.58e-10
                           10        20
                   ....*....|....*....|....*....
gi 1958680058 1267 EESIFPDGTIVRVQRDGNKIIEFNNGQRE 1295
Cdd:pfam07202    1 EEIIFPDGTVERVYSDGDKVIEFPNGTRE 29
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 905-1140 9.97e-09

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 60.08  E-value: 9.97e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  905 LREKVIELESEIEKFKAENTSLAKLRIERESALEKLRKEIADFEQQKARElaRIEEyKKEETRKLQKERKVFEKYTAA-- 982
Cdd:TIGR02169  742 LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHS--RIPE-IQAELSKLEEEVSRIEARLREie 818

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  983 ----ARTFPDKKEREEIQALKQQIQELQEDLKRKETKWSSTHGRLR---SQIEMLVKENTDLREEIKVMERFRLEAWKRA 1055
Cdd:TIGR02169  819 qklnRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEeleEELEELEAALRDLESRLGDLKKERDELEAQL 898

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058 1056 EAIENspkacqyimatkKDESMNSSIQFQKSHASLGVQGEKYKKKYLPAQGNSSRRSKSVPPRDLgSLDKGQAALPR--- 1132
Cdd:TIGR02169  899 RELER------------KIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEEL-SLEDVQAELQRvee 965

                          250
                   ....*....|
gi 1958680058 1133 --EPLQPVNF 1140
Cdd:TIGR02169  966 eiRALEPVNM 975
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 903-1060 5.37e-08

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 57.64  E-value: 5.37e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  903 QVLREKVIELESEIEKFKAENTSLAKLRIERESALEKLRKEIADFEQQKARELARIEEYKKEETRKLQKERKVFEKYTAA 982
Cdd:COG1196    235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958680058  983 ARTfpDKKEREEIQALKQQIQELQEDLKRKETKWSSTHGRLRSQIEMLVKENTDLREEIKVMERFRLEAWKRAEAIEN 1060
Cdd:COG1196    315 EER--LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
905-1048 3.41e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 51.60  E-value: 3.41e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  905 LREKVIELESEIEKFKAENTSLAKLRIERESALEKLRKEIADFEqQKARELARIEEyKKEETRKLQKERkvfEKYTAAAR 984
Cdd:PRK03918   236 LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELE-EKVKELKELKE-KAEEYIKLSEFY---EEYLDELR 310

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958680058  985 TFPDKKER--EEIQALKQQIQELQEDLKRKEtkwssthgRLRSQIEMLVKENTDLREEIKVMERFR 1048
Cdd:PRK03918   311 EIEKRLSRleEEINGIEERIKELEEKEERLE--------ELKKKLKELEKRLEELEERHELYEEAK 368
Tcp10_C pfam07202
T-complex protein 10 C-terminus; This entry represents a repeating unit commonly found in the ...
 1231-1259 3.88e-05

T-complex protein 10 C-terminus; This entry represents a repeating unit commonly found in the C terminus of the eukaryotic T-complex protein 10. The T-complex is involved in spermatogenesis in mice. The repeating unit is commonly found 3-4 times, but there is often a gap between the first and second repeats, which is big enough to accommodate another repeat unit. However, the score is insufficient to be included, and could be a degenerate repeat.


Pssm-ID: 462118  Cd Length: 30  Bit Score: 41.65  E-value: 3.88e-05
                           10        20
                   ....*....|....*....|....*....
gi 1958680058 1231 EVLHFSSGQIEKHFPDGRKEITFPDQTIK 1259
Cdd:pfam07202    1 EEIIFPDGTVERVYSDGDKVIEFPNGTRE 29
Tcp10_C pfam07202
T-complex protein 10 C-terminus; This entry represents a repeating unit commonly found in the ...
 1302-1331 9.57e-05

T-complex protein 10 C-terminus; This entry represents a repeating unit commonly found in the C terminus of the eukaryotic T-complex protein 10. The T-complex is involved in spermatogenesis in mice. The repeating unit is commonly found 3-4 times, but there is often a gap between the first and second repeats, which is big enough to accommodate another repeat unit. However, the score is insufficient to be included, and could be a degenerate repeat.


Pssm-ID: 462118  Cd Length: 30  Bit Score: 40.49  E-value: 9.57e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 1958680058 1302 KRREYPDGTVKTVYANGHQETKYTSGRVRV 1331
Cdd:pfam07202    1 EEIIFPDGTVERVYSDGDKVIEFPNGTREI 30
alph_xenorhab_B NF033927
alpha-xenorhabdolysin family binary toxin subunit B;
911-1061 1.64e-04

alpha-xenorhabdolysin family binary toxin subunit B;


Pssm-ID: 411488 [Multi-domain]  Cd Length: 223  Bit Score: 44.54  E-value: 1.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  911 ELESEIEKFKAENTSLAKLRIERESA--LEKLRKEIADFEQQKARELARIEEYKkEETRKLQKERKVFEKYTAAAR---T 985
Cdd:NF033927     8 ALRKSAAKIANKLDDLSQINLREATLdlLAQLQEQIAELEAQIAALESKLNELA-EDRKVIIEAIDLIEKYNIADLfkdL 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  986 FPDKkerEEIQAL------KQQIQELQEDLKRKETKWSS---------THGRLRSQIEMLVKENTDLREEIKVMErFRLE 1050
Cdd:NF033927    87 LPTA---EEIDSLglpppeKDLVKAAIERLKKLLGKISEgltyidlveARDKLRDRINALLAESRTLDKDIKALA-GKLE 162

                          170
                   ....*....|.
gi 1958680058 1051 AWKRAEAIENS 1061
Cdd:NF033927   163 ELTAIAAIDEE 173
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 907-1004 4.90e-04

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 41.79  E-value: 4.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  907 EKVIElesEIEKFKAENTSLAKLRIERESALEKLRKEIADFEQQKARELARIEEYKKEETRKLQKERKVFEKYTAAARTF 986
Cdd:pfam03938    8 QKILE---ESPEGKAAQAQLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQQE 84

                           90
                   ....*....|....*...
gi 1958680058  987 PDKKEREEIQALKQQIQE 1004
Cdd:pfam03938   85 LQKKQQELLQPIQDKINK 102
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 905-1041 6.15e-03

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 40.43  E-value: 6.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  905 LREKVIELESEIEKFKAENTSlaklrieRESALEKLRKEIADF--EQQKARELARIEEYKKEetrkLQKERKvfeKYTAA 982
Cdd:cd22656    133 YQDKAAKVVDKLTDFENQTEK-------DQTALETLEKALKDLltDEGGAIARKEIKDLQKE----LEKLNE---EYAAK 198

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958680058  983 ARtfpdkkerEEIQALKQQIQELQEDLKRKEtkwssthgRLRSQIEMLVKENTDLREEI 1041
Cdd:cd22656    199 LK--------AKIDELKALIADDEAKLAAAL--------RLIADLTAADTDLDNLLALI 241
 
Name Accession Description Interval E-value
Tcp10_C pfam07202
T-complex protein 10 C-terminus; This entry represents a repeating unit commonly found in the ...
 1158-1186 4.99e-11

T-complex protein 10 C-terminus; This entry represents a repeating unit commonly found in the C terminus of the eukaryotic T-complex protein 10. The T-complex is involved in spermatogenesis in mice. The repeating unit is commonly found 3-4 times, but there is often a gap between the first and second repeats, which is big enough to accommodate another repeat unit. However, the score is insufficient to be included, and could be a degenerate repeat.


Pssm-ID: 462118  Cd Length: 30  Bit Score: 58.21  E-value: 4.99e-11
                           10        20
                   ....*....|....*....|....*....
gi 1958680058 1158 EINHPDGKVEKVYKNGCRVVLFPNGTRKE 1186
Cdd:pfam07202    2 EIIFPDGTVERVYSDGDKVIEFPNGTREI 30
Tcp10_C pfam07202
T-complex protein 10 C-terminus; This entry represents a repeating unit commonly found in the ...
 1267-1295 5.58e-10

T-complex protein 10 C-terminus; This entry represents a repeating unit commonly found in the C terminus of the eukaryotic T-complex protein 10. The T-complex is involved in spermatogenesis in mice. The repeating unit is commonly found 3-4 times, but there is often a gap between the first and second repeats, which is big enough to accommodate another repeat unit. However, the score is insufficient to be included, and could be a degenerate repeat.


Pssm-ID: 462118  Cd Length: 30  Bit Score: 55.52  E-value: 5.58e-10
                           10        20
                   ....*....|....*....|....*....
gi 1958680058 1267 EESIFPDGTIVRVQRDGNKIIEFNNGQRE 1295
Cdd:pfam07202    1 EEIIFPDGTVERVYSDGDKVIEFPNGTRE 29
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 905-1140 9.97e-09

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 60.08  E-value: 9.97e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  905 LREKVIELESEIEKFKAENTSLAKLRIERESALEKLRKEIADFEQQKARElaRIEEyKKEETRKLQKERKVFEKYTAA-- 982
Cdd:TIGR02169  742 LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHS--RIPE-IQAELSKLEEEVSRIEARLREie 818

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  983 ----ARTFPDKKEREEIQALKQQIQELQEDLKRKETKWSSTHGRLR---SQIEMLVKENTDLREEIKVMERFRLEAWKRA 1055
Cdd:TIGR02169  819 qklnRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEeleEELEELEAALRDLESRLGDLKKERDELEAQL 898

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058 1056 EAIENspkacqyimatkKDESMNSSIQFQKSHASLGVQGEKYKKKYLPAQGNSSRRSKSVPPRDLgSLDKGQAALPR--- 1132
Cdd:TIGR02169  899 RELER------------KIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEEL-SLEDVQAELQRvee 965

                          250
                   ....*....|
gi 1958680058 1133 --EPLQPVNF 1140
Cdd:TIGR02169  966 eiRALEPVNM 975
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 903-1060 5.37e-08

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 57.64  E-value: 5.37e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  903 QVLREKVIELESEIEKFKAENTSLAKLRIERESALEKLRKEIADFEQQKARELARIEEYKKEETRKLQKERKVFEKYTAA 982
Cdd:COG1196    235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958680058  983 ARTfpDKKEREEIQALKQQIQELQEDLKRKETKWSSTHGRLRSQIEMLVKENTDLREEIKVMERFRLEAWKRAEAIEN 1060
Cdd:COG1196    315 EER--LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
897-1046 7.69e-08

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 57.23  E-value: 7.69e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  897 GDSVRSQVLREKVIELESEIEKFKAENTSLAKLRIERESALEKLRKEIADFEQQKA----RELARIEEYKKEETRKLQKE 972
Cdd:COG4913    278 RAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRgnggDRLEQLEREIERLERELEER 357

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958680058  973 RKVFEKYTAAART--FPDKKEREEIQALKQQIQELQEDLKRKETKWSSTHGRLRSQIEMLVKENTDLREEIKVMER 1046
Cdd:COG4913    358 ERRRARLEALLAAlgLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 903-1060 1.04e-07

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.87  E-value: 1.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  903 QVLREKVIELESEIEKFKAENTSLAKLRIERESALEKLRKEIADFEQQKARELARIEEYKKEETRKLQKERKVFEKYTAA 982
Cdd:COG1196    291 YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  983 ARTFPDKKE-----REEIQALKQQIQELQEDLKRKETKWSSTHGRLRSQIEMLVKENTDLREEIKVMERFRLEAWKRAEA 1057
Cdd:COG1196    371 EAELAEAEEeleelAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450


                   ...
gi 1958680058 1058 IEN 1060
Cdd:COG1196    451 EAE 453
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
903-1057 1.95e-07

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 55.63  E-value: 1.95e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  903 QVLREKVIELESEIEKFKAENTSLaklrierESALEKLRKEIADFEqqkarelARIEEYKKEETRKLQKERKVfekytaa 982
Cdd:COG2433    409 TEEEEEIRRLEEQVERLEAEVEEL-------EAELEEKDERIERLE-------RELSEARSEERREIRKDREI------- 467

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958680058  983 artfpdKKEREEIQALKQQIQELQEDLKRKETKWSsthgRLRSQIEMLVKENTdlrEEIKVMERFRLEAWKRAEA 1057
Cdd:COG2433    468 ------SRLDREIERLERELEEERERIEELKRKLE----RLKELWKLEHSGEL---VPVKVVEKFTKEAIRRLEE 529
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 901-1058 4.24e-07

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 54.68  E-value: 4.24e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  901 RSQVLREKVIELESEIEKFKAENTSLAKLRIERESALEKLRKEIADFEQQKARELARIEEYKKEETRkLQKERKVFEKYT 980
Cdd:TIGR02168  345 KLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLER-LEDRRERLQQEI 423

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  981 AAARTFPDKKEREEIQA----LKQQIQELQEDLKRKETKWSSTHGRLRSQIEMLVKENTDLRE---EIKVMERFRLEAWK 1053
Cdd:TIGR02168  424 EELLKKLEEAELKELQAeleeLEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQlqaRLDSLERLQENLEG 503


                   ....*
gi 1958680058 1054 RAEAI 1058
Cdd:TIGR02168  504 FSEGV 508
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 901-1060 5.29e-07

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.56  E-value: 5.29e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  901 RSQVLREKVIELESEIEKFKAENTSLAKLRIERESALEKLRKEIADFEQQKARELARIEEYKKEETRKLQKERkvfekyt 980
Cdd:COG1196    254 ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELA------- 326

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  981 aaartfpdkKEREEIQALKQQIQELQEDLKRKETKWSSTHGRLRSQIEMLVKENTDLREEIKVMERFRLEAWKRAEAIEN 1060
Cdd:COG1196    327 ---------ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 905-1045 8.98e-07

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 51.46  E-value: 8.98e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  905 LREKVIELESEIEKFKAENTSLAKLRIERESALEKLRKEIADFEQQKARELARIEEYKKE-ETRKLQKERKVFEK---YT 980
Cdd:COG1579     22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlGNVRNNKEYEALQKeieSL 101

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958680058  981 AAARTFPDKKERE---EIQALKQQIQELQEDLKRKETKWSSTHGRLRSQIEMLVKENTDLREEIKVME 1045
Cdd:COG1579    102 KRRISDLEDEILElmeRIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELA 169
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
894-1054 9.38e-07

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 53.23  E-value: 9.38e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  894 QPPGDSVRSQVLREKVIELESEIEKFKAENTSLAKLRIERESA---LEKLRKEIADFEQQKA-----RELARIEEYKKEE 965
Cdd:COG4717     65 KPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELeaeLEELREELEKLEKLLQllplyQELEALEAELAEL 144

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  966 TRKLQKERKVFEKYTAAartfpdkkeREEIQALKQQIQELQEDLKRKETKWSSTHgrlRSQIEMLVKENTDLREEIKVME 1045
Cdd:COG4717    145 PERLEELEERLEELREL---------EEELEELEAELAELQEELEELLEQLSLAT---EEELQDLAEELEELQQRLAELE 212


                   ....*....
gi 1958680058 1046 RfRLEAWKR 1054
Cdd:COG4717    213 E-ELEEAQE 220
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 901-1060 2.39e-06

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.25  E-value: 2.39e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  901 RSQVLREKVIELESEIEKFKAENTSLAKLRIERESALEKLRKEIADFEQQKARELARIEEykkEETRKLQKERKVFEKYT 980
Cdd:COG1196    310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE---AEAELAEAEEELEELAE 386

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  981 AAARtfPDKKEREEIQALKQQIQELQEDLKRKEtkwssthgRLRSQIEMLVKENTDLREEIKVMERFRLEAWKRAEAIEN 1060
Cdd:COG1196    387 ELLE--ALRAAAELAAQLEELEEAEEALLERLE--------RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 911-1061 2.72e-06

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.98  E-value: 2.72e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  911 ELESEIEKFKAENTSLAKLRIERESALEKLRKEIADFEQQKARELARIEEYKKEETRKLQKERKVFEKYTAAARTFPDK- 989
Cdd:TIGR02168  681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELe 760

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  990 -----------KEREEIQALKQQIQELQEDLKRKE---TKWSSTHGRLRSQIEMLVKENTDLREEIKVMERFRLEAWKRA 1055
Cdd:TIGR02168  761 aeieeleerleEAEEELAEAEAEIEELEAQIEQLKeelKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRL 840


                   ....*.
gi 1958680058 1056 EAIENS 1061
Cdd:TIGR02168  841 EDLEEQ 846
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 899-1057 3.31e-06

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.98  E-value: 3.31e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  899 SVRSQVLREKVIELESEIEKFKAENTSLAKLRIERESALEKLRKEIADFEQQKARELARIEEYKKEETRKLQKERKVFEK 978
Cdd:TIGR02168  816 NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSE 895

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958680058  979 YTAAARTFpdKKEREEIQALKQQIQELQEDLKRKETKWSSTHGRLRSQIEMLVKENTDLREEIKVMERFRLEAWKRAEA 1057
Cdd:TIGR02168  896 LEELSEEL--RELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARR 972
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
905-1048 3.41e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 51.60  E-value: 3.41e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  905 LREKVIELESEIEKFKAENTSLAKLRIERESALEKLRKEIADFEqQKARELARIEEyKKEETRKLQKERkvfEKYTAAAR 984
Cdd:PRK03918   236 LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELE-EKVKELKELKE-KAEEYIKLSEFY---EEYLDELR 310

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958680058  985 TFPDKKER--EEIQALKQQIQELQEDLKRKEtkwssthgRLRSQIEMLVKENTDLREEIKVMERFR 1048
Cdd:PRK03918   311 EIEKRLSRleEEINGIEERIKELEEKEERLE--------ELKKKLKELEKRLEELEERHELYEEAK 368
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
905-1073 4.11e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 51.60  E-value: 4.11e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  905 LREKVIELESEIEKFKAENTSLAKLRIEresaLEKLRKEIADFEQQKARELARIEEyKKEETRKLQKERKVFEKYTaaar 984
Cdd:PRK03918   219 LREELEKLEKEVKELEELKEEIEELEKE----LESLEGSKRKLEEKIRELEERIEE-LKKEIEELEEKVKELKELK---- 289

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  985 tfPDKKEREEIQALKQQIQELQEDLKRKETKWSSthgrLRSQIEMLVKENTDLREEIKVMERFRLEAWKRAEAIENSPKA 1064
Cdd:PRK03918   290 --EKAEEYIKLSEFYEEYLDELREIEKRLSRLEE----EINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHEL 363


                   ....*....
gi 1958680058 1065 CQYIMATKK 1073
Cdd:PRK03918   364 YEEAKAKKE 372
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 905-1068 5.39e-06

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.09  E-value: 5.39e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  905 LREKVIELESEIEKFKAENTSLAKLRIERESALEKLRKEIADFEQQKARELARIEEYKKEETRKLQKERKVFEKYTAAAR 984
Cdd:COG1196    363 AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  985 TF-PDKKEREEIQALKQQIQELQEDLKRKETKWSSTHGRLRSQIEMLVKENTDLREEIKVMERFrLEAWKRAEAIENSPK 1063
Cdd:COG1196    443 ALeEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGF-LEGVKAALLLAGLRG 521


                   ....*
gi 1958680058 1064 ACQYI 1068
Cdd:COG1196    522 LAGAV 526
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
903-1056 8.18e-06

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.15  E-value: 8.18e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  903 QVLREKVIELESEIEKFKAENTSLAKLRIER-ESALEKLRKEIADFeQQKARELARIEEYKKEETRKLQKERKVFEKYTA 981
Cdd:COG4717     45 AMLLERLEKEADELFKPQGRKPELNLKELKElEEELKEAEEKEEEY-AELQEELEELEEELEELEAELEELREELEKLEK 123

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958680058  982 AARTFPDKKEREEIQALKQQIQELQEDLKRKETKWSsthgRLRSQIEMLVKENTDLREEI-KVMERFRLEAWKRAE 1056
Cdd:COG4717    124 LLQLLPLYQELEALEAELAELPERLEELEERLEELR----ELEEELEELEAELAELQEELeELLEQLSLATEEELQ 195
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 907-1061 1.39e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.55  E-value: 1.39e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  907 EKVIELESEIEKFKAEntsLAKLRIE-RESALEKLRKEIADFEQQKARELARIEEYKKEETR---KLQKERKVFEKYTAA 982
Cdd:COG1196    213 ERYRELKEELKELEAE---LLLLKLReLEAELEELEAELEELEAELEELEAELAELEAELEElrlELEELELELEEAQAE 289

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958680058  983 ARtfpdkKEREEIQALKQQIQELQEDLKRKEtkwsSTHGRLRSQIEMLVKENTDLREEIKVMERFRLEAWKRAEAIENS 1061
Cdd:COG1196    290 EY-----ELLAELARLEQDIARLEERRRELE----ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 905-1055 2.98e-05

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.51  E-value: 2.98e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  905 LREKVIELESEIEKFKAENTSLAKLRIERESALEKLRKEIADFEQQKARELARIE----EYKKEETRKLQKERKVFEKYT 980
Cdd:TIGR02168  258 LTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAnlerQLEELEAQLEELESKLDELAE 337

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  981 AAARTFPD---------------KKEREEIQALKQQIQELQE----------DLKRKETKWSSTHGRLRSQIEMLVKENT 1035
Cdd:TIGR02168  338 ELAELEEKleelkeelesleaelEELEAELEELESRLEELEEqletlrskvaQLELQIASLNNEIERLEARLERLEDRRE 417

                          170       180
                   ....*....|....*....|
gi 1958680058 1036 DLREEIKVMERFRLEAWKRA 1055
Cdd:TIGR02168  418 RLQQEIEELLKKLEEAELKE 437
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
905-1042 3.20e-05

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 48.47  E-value: 3.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  905 LREKVIELESEIEKFKAEN--TSLAKLRIERESALEKLRKEIADFEQQKARELARIEEYKKEETRKLQkerkvfekytaa 982
Cdd:COG3206    187 LRKELEEAEAALEEFRQKNglVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPD------------ 254

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958680058  983 arTFPDKKEREEIQALKQQIQELQEDLKRKETKWSSTH---GRLRSQIEMLvkeNTDLREEIK 1042
Cdd:COG3206    255 --ALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHpdvIALRAQIAAL---RAQLQQEAQ 312
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 925-1063 3.35e-05

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 48.28  E-value: 3.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  925 SLAKLRIERESALEKLRKEIADFEQQKARELARIEEYKKEETRKLQKERKVFEKYTAAArtfpdKKEREE-IQALKQQIQ 1003
Cdd:PRK00409   524 SLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEA-----KKEADEiIKELRQLQK 598

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958680058 1004 ELQEDLKRKETKwsSTHGRLRSQIEML---VKENTDLREEIKVMERFRLEAW-KRAEAIENSPK 1063
Cdd:PRK00409   599 GGYASVKAHELI--EARKRLNKANEKKekkKKKQKEKQEELKVGDEVKYLSLgQKGEVLSIPDD 660
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 899-1042 3.71e-05

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 48.53  E-value: 3.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  899 SVRSQVLREKVIELESEIEKFKAENTSLAKLRIERESALEKLRKEIADFEQqkarELARIEEYKKE-ETRKLQKERKVFE 977
Cdd:TIGR02169  377 DKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNA----AIAGIEAKINElEEEKEDKALEIKK 452

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958680058  978 KYTAAARTFPD-KKEREEIQALKQQIQELQEDLKRKETKWSSTHGRlRSQIEMLVKENTDLREEIK 1042
Cdd:TIGR02169  453 QEWKLEQLAADlSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQ-ARASEERVRGGRAVEEVLK 517
Tcp10_C pfam07202
T-complex protein 10 C-terminus; This entry represents a repeating unit commonly found in the ...
 1231-1259 3.88e-05

T-complex protein 10 C-terminus; This entry represents a repeating unit commonly found in the C terminus of the eukaryotic T-complex protein 10. The T-complex is involved in spermatogenesis in mice. The repeating unit is commonly found 3-4 times, but there is often a gap between the first and second repeats, which is big enough to accommodate another repeat unit. However, the score is insufficient to be included, and could be a degenerate repeat.


Pssm-ID: 462118  Cd Length: 30  Bit Score: 41.65  E-value: 3.88e-05
                           10        20
                   ....*....|....*....|....*....
gi 1958680058 1231 EVLHFSSGQIEKHFPDGRKEITFPDQTIK 1259
Cdd:pfam07202    1 EEIIFPDGTVERVYSDGDKVIEFPNGTRE 29
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
903-1064 7.35e-05

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.22  E-value: 7.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  903 QVLREKVIELESEIEKFKAENTSLAKLR---IERESALEKLRKeiADFEQQKARELAR-IEEyKKEETRKLQKERKVFEK 978
Cdd:COG4913    613 AALEAELAELEEELAEAEERLEALEAELdalQERREALQRLAE--YSWDEIDVASAEReIAE-LEAELERLDASSDDLAA 689

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  979 YTAAArtfpdKKEREEIQALKQQIQELQEDLKRKETKWSsthgRLRSQIEMLVKENTDLREEIKVMERFRLEAWKRAEAI 1058
Cdd:COG4913    690 LEEQL-----EELEAELEELEEELDELKGEIGRLEKELE----QAEEELDELQDRLEAAEDLARLELRALLEERFAAALG 760


                   ....*.
gi 1958680058 1059 ENSPKA 1064
Cdd:COG4913    761 DAVERE 766
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
900-1051 8.56e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.98  E-value: 8.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  900 VRSQVLREKVIELESEIEKFKAENTSLAKLRIEresaLEKLRKEIADFEQQKARELARIEEYKKEETRKLQ-------KE 972
Cdd:PRK03918   141 LESDESREKVVRQILGLDDYENAYKNLGEVIKE----IKRRIERLEKFIKRTENIEELIKEKEKELEEVLReineissEL 216

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  973 RKVFEKYTAAARTFPDKKE-REEIQALKQQIQELQEDLKRKETKWssthGRLRSQIEMLVKENTDLREEIKVMERFRLEA 1051
Cdd:PRK03918   217 PELREELEKLEKEVKELEElKEEIEELEKELESLEGSKRKLEEKI----RELEERIEELKKEIEELEEKVKELKELKEKA 292
Tcp10_C pfam07202
T-complex protein 10 C-terminus; This entry represents a repeating unit commonly found in the ...
 1302-1331 9.57e-05

T-complex protein 10 C-terminus; This entry represents a repeating unit commonly found in the C terminus of the eukaryotic T-complex protein 10. The T-complex is involved in spermatogenesis in mice. The repeating unit is commonly found 3-4 times, but there is often a gap between the first and second repeats, which is big enough to accommodate another repeat unit. However, the score is insufficient to be included, and could be a degenerate repeat.


Pssm-ID: 462118  Cd Length: 30  Bit Score: 40.49  E-value: 9.57e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 1958680058 1302 KRREYPDGTVKTVYANGHQETKYTSGRVRV 1331
Cdd:pfam07202    1 EEIIFPDGTVERVYSDGDKVIEFPNGTREI 30
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
922-1040 1.16e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 46.57  E-value: 1.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  922 ENTSLAKLRIER-----ESALEKLRKEIADFEQQKARE-LARIEEYKKEETRKL-----QKERKVFEKYTAAARTFPDKK 990
Cdd:PRK02224   169 ERASDARLGVERvlsdqRGSLDQLKAQIEEKEEKDLHErLNGLESELAELDEEIeryeeQREQARETRDEADEVLEEHEE 248

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958680058  991 EREEIQALKQQIQELQEDLKRKETKWSSTHGR---LRSQIEMLVKENTDLREE 1040
Cdd:PRK02224   249 RREELETLEAEIEDLRETIAETEREREELAEEvrdLRERLEELEEERDDLLAE 301
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
905-1060 1.22e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.60  E-value: 1.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  905 LREKVIELESEIEKFKAENTSLAKL---RIERESALEKLRKEIADFEQQKA-----------RELARIEEYKKE--ETRK 968
Cdd:PRK03918   530 LKEKLIKLKGEIKSLKKELEKLEELkkkLAELEKKLDELEEELAELLKELEelgfesveeleERLKELEPFYNEylELKD 609

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  969 LQKERKVFEKYTAAARTFPDKKeREEIQALKQQIQELQEDLKRKETKWS-STHGRLRSQIEMLVKENTDLREEIKVMERF 1047
Cdd:PRK03918   610 AEKELEREEKELKKLEEELDKA-FEELAETEKRLEELRKELEELEKKYSeEEYEELREEYLELSRELAGLRAELEELEKR 688

                          170
                   ....*....|...
gi 1958680058 1048 RLEAWKRAEAIEN 1060
Cdd:PRK03918   689 REEIKKTLEKLKE 701
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 887-1014 1.25e-04

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 46.61  E-value: 1.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  887 KLSLSQDQPPGDSvrsQVLREKVIELESEIEKFKAENTSLAKLRieresaLEKLRKEIADFEQQKARELARIEEyKKEET 966
Cdd:COG0542    401 RVRMEIDSKPEEL---DELERRLEQLEIEKEALKKEQDEASFER------LAELRDELAELEEELEALKARWEA-EKELI 470

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1958680058  967 RKLQKERKVFEkytaaartfpdkKEREEIQALKQQIQELQEDLKRKET 1014
Cdd:COG0542    471 EEIQELKEELE------------QRYGKIPELEKELAELEEELAELAP 506
alph_xenorhab_B NF033927
alpha-xenorhabdolysin family binary toxin subunit B;
911-1061 1.64e-04

alpha-xenorhabdolysin family binary toxin subunit B;


Pssm-ID: 411488 [Multi-domain]  Cd Length: 223  Bit Score: 44.54  E-value: 1.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  911 ELESEIEKFKAENTSLAKLRIERESA--LEKLRKEIADFEQQKARELARIEEYKkEETRKLQKERKVFEKYTAAAR---T 985
Cdd:NF033927     8 ALRKSAAKIANKLDDLSQINLREATLdlLAQLQEQIAELEAQIAALESKLNELA-EDRKVIIEAIDLIEKYNIADLfkdL 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  986 FPDKkerEEIQAL------KQQIQELQEDLKRKETKWSS---------THGRLRSQIEMLVKENTDLREEIKVMErFRLE 1050
Cdd:NF033927    87 LPTA---EEIDSLglpppeKDLVKAAIERLKKLLGKISEgltyidlveARDKLRDRINALLAESRTLDKDIKALA-GKLE 162

                          170
                   ....*....|.
gi 1958680058 1051 AWKRAEAIENS 1061
Cdd:NF033927   163 ELTAIAAIDEE 173
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
905-1020 3.51e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.14  E-value: 3.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  905 LREKVIELESEIEKFKAENTSLAklriERESALEKLRKEIADFEQQKARELARIEEYKKEETRKLQKERKVFEKYTAAAr 984
Cdd:COG4717    137 LEAELAELPERLEELEERLEELR----ELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAEL- 211

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1958680058  985 tfpdkkeREEIQALKQQIQELQEDLKRKETKWSSTH 1020
Cdd:COG4717    212 -------EEELEEAQEELEELEEELEQLENELEAAA 240
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
898-1053 3.76e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.91  E-value: 3.76e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  898 DSVRSQVLREKVIELESEIEKFKAENTSLAKLrierESALEKLRKEIADFEQQKARelarieeyKKEETRKLQKERKVFE 977
Cdd:COG4913    659 DEIDVASAEREIAELEAELERLDASSDDLAAL----EEQLEELEAELEELEEELDE--------LKGEIGRLEKELEQAE 726

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  978 ----KYTAAARTFPDKKEREEIQALKQQIQELQEDLKRKETKwssthGRLRSQIEMLVKENTDLREEI-KVMERFRlEAW 1052
Cdd:COG4913    727 eeldELQDRLEAAEDLARLELRALLEERFAAALGDAVERELR-----ENLEERIDALRARLNRAEEELeRAMRAFN-REW 800


                   .
gi 1958680058 1053 K 1053
Cdd:COG4913    801 P 801
PTZ00121 PTZ00121
MAEBL; Provisional
 907-1106 4.64e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 4.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  907 EKVIELESEIEKFKAEN---TSLAKLRIERESALEKLRKEIADFEQQKARELARIEEYKKEEtrklqkERKVFEKYTAAA 983
Cdd:PTZ00121  1595 EEVMKLYEEEKKMKAEEakkAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAE------EENKIKAAEEAK 1668

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  984 RTFPDKKEREEIQALKQQIQELQEDLKRKETKWSSTHgRLRSQIEMLVKENTDLREEIKVmERFRLEAWKRaEAIENSPK 1063
Cdd:PTZ00121  1669 KAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAE-ELKKKEAEEKKKAEELKKAEEE-NKIKAEEAKK-EAEEDKKK 1745

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1958680058 1064 ACQyimaTKKDESMNSSIQFQKSHASLGVQGEKYKKKYLPAQG 1106
Cdd:PTZ00121  1746 AEE----AKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEE 1784
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 907-1004 4.90e-04

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 41.79  E-value: 4.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  907 EKVIElesEIEKFKAENTSLAKLRIERESALEKLRKEIADFEQQKARELARIEEYKKEETRKLQKERKVFEKYTAAARTF 986
Cdd:pfam03938    8 QKILE---ESPEGKAAQAQLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQQE 84

                           90
                   ....*....|....*...
gi 1958680058  987 PDKKEREEIQALKQQIQE 1004
Cdd:pfam03938   85 LQKKQQELLQPIQDKINK 102
PRK12704 PRK12704
phosphodiesterase; Provisional
 906-1058 5.15e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.38  E-value: 5.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  906 REKVIELESEIEKFKAEntsLAKLRIERESALEKLRKEIADFEQQKARELARIEeyKKEEtrKLQKERKVFEkytaaart 985
Cdd:PRK12704    56 KEALLEAKEEIHKLRNE---FEKELRERRNELQKLEKRLLQKEENLDRKLELLE--KREE--ELEKKEKELE-------- 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  986 fpdkKEREEIQALKQQIQELQEDLKRKETKWSS-THGRLRSQI-EMLVKEntdLREEI-----KVMERFRLEAWKRAEAI 1058
Cdd:PRK12704   121 ----QKQQELEKKEEELEELIEEQLQELERISGlTAEEAKEILlEKVEEE---ARHEAavlikEIEEEAKEEADKKAKEI 193
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 911-1046 5.87e-04

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 44.35  E-value: 5.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  911 ELESEIEKFKAENTSLAKLRiERESALEKLRKEIADFEQQKARELARIEEYKKEETRKLQKERKV---FEKYTAAARTFP 987
Cdd:pfam05557   42 QLDRESDRNQELQKRIRLLE-KREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADAREViscLKNELSELRRQI 120

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958680058  988 DKKErEEIQALKQQIQELQEDLKRKETKWSStHGRLRSQIEMLVKENTDLREEIKVMER 1046
Cdd:pfam05557  121 QRAE-LELQSTNSELEELQERLDLLKAKASE-AEQLRQNLEKQQSSLAEAEQRIKELEF 177
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 911-1059 6.57e-04

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 44.29  E-value: 6.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  911 ELESEIEKFKAENTSLAKLRIERESALEKLRKEIADFEQQKARELARIEEYKKEETRKLQKERKVFEKYTAAARTFPDKK 990
Cdd:TIGR02169  234 ALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEK 313

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958680058  991 EReEIQALKQQIQELQEDLKRKEtkwsSTHGRLRSQIEMLVKENTDLREEIKVMERFRLEAWKRAEAIE 1059
Cdd:TIGR02169  314 ER-ELEDAEERLAKLEAEIDKLL----AEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVD 377
PTZ00121 PTZ00121
MAEBL; Provisional
 906-1100 6.73e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 6.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  906 REKVIELESEIEKFKAENTSLAKLRIERESALEKLRKEIADfEQQKARELARIEEYKKEETRKLQKERKVFEKYTAAART 985
Cdd:PTZ00121  1509 KKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKAD-ELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAK 1587

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  986 FPDKKEREEIQALKQQIQELQEDLKRKETKWSSTHGRLRSQIEmlVKENTDLREEIKVMERFRLEAWKRAEAiENSPKAC 1065
Cdd:PTZ00121  1588 KAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEE--EKKKVEQLKKKEAEEKKKAEELKKAEE-ENKIKAA 1664

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1958680058 1066 QyiMATKKDESMNSSIQFQKSHASLGVQGEKYKKK 1100
Cdd:PTZ00121  1665 E--EAKKAEEDKKKAEEAKKAEEDEKKAAEALKKE 1697
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
905-1066 7.50e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.90  E-value: 7.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  905 LREKVIELESEIEKFKAENTSLAKLrIERESALEKLRK----------EIADFEQQKARELARIEEYKKEETRKLQKERK 974
Cdd:PRK03918   464 IEKELKEIEEKERKLRKELRELEKV-LKKESELIKLKElaeqlkeleeKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIK 542

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  975 VFekytaaartfpdKKEREEIQALKQQIQELQEDLKRKETKWSSTHGRLRsqiEMLVKENTDLREEIKVMERFRLE---- 1050
Cdd:PRK03918   543 SL------------KKELEKLEELKKKLAELEKKLDELEEELAELLKELE---ELGFESVEELEERLKELEPFYNEylel 607

                          170
                   ....*....|....*...
gi 1958680058 1051 --AWKRAEAIENSPKACQ 1066
Cdd:PRK03918   608 kdAEKELEREEKELKKLE 625
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 895-1078 8.68e-04

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.90  E-value: 8.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  895 PPGDSVRSQVLREKVIELESEIEKFKAENTSLAKLRIERESALEKLRKEIADFEqqkaRELARIEEYKKEETRKLqKERK 974
Cdd:TIGR02169  669 SRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIE----KEIEQLEQEEEKLKERL-EELE 743

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  975 VFEKYTAAARTfpdkKEREEIQALKQQIQELQEDLKRKETKWSSTHGRL-RSQIEMLVKENTDLREEIKvmerfRLEAwk 1053
Cdd:TIGR02169  744 EDLSSLEQEIE----NVKSELKELEARIEELEEDLHKLEEALNDLEARLsHSRIPEIQAELSKLEEEVS-----RIEA-- 812

                          170       180
                   ....*....|....*....|....*
gi 1958680058 1054 RAEAIENSPKACQYIMATKKDESMN 1078
Cdd:TIGR02169  813 RLREIEQKLNRLTLEKEYLEKEIQE 837
COG5644 COG5644
U3 small nucleolar RNA-associated protein 14 [Function unknown];
891-1041 9.44e-04

U3 small nucleolar RNA-associated protein 14 [Function unknown];


Pssm-ID: 227931 [Multi-domain]  Cd Length: 869  Bit Score: 43.54  E-value: 9.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  891 SQDQPPGDSVRS--QVLREKVIELESEIEKFkaENTSLAKLRIE--RESALE-KLRKEIADFEQQKARELARIeeyKKEE 965
Cdd:COG5644    328 SSFEPRTESERKmhQALLDAGLENESALKKQ--EELALNKLSVEevAERTRQlRFMRELMFREERKAKRVAKI---KSKT 402

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958680058  966 TRKLQKERKVFEKYTAAARTFPDKKEREEIQALKQQIQELQEDLK--RKETKWSSTHGRLRSQIEMLVKENTDLREEI 1041
Cdd:COG5644    403 YRKIRKNRKEKEMALIPKSEDLENEKSEEARALERMTQRHKNTSSwtRKMLERASHGEGTREAVNEQIRKGDELMQRI 480
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 901-1071 1.24e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 43.19  E-value: 1.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  901 RSQVLREKVIELES-EIEKFKAENTSLAKLRIERESALEKLRKEIADFEQQ--------KARELARIEEYKKEETRKLQK 971
Cdd:pfam17380  411 RQRKIQQQKVEMEQiRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQverlrqqeEERKRKKLELEKEKRDRKRAE 490

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  972 E--RKVFEKYTAAARTFPDKKEREEiQALKQQIQELQEDLKRKETKWSSTHGRlRSQIEMlvKENTDLREEIKVM--ERF 1047
Cdd:pfam17380  491 EqrRKILEKELEERKQAMIEEERKR-KLLEKEMEERQKAIYEEERRREAEEER-RKQQEM--EERRRIQEQMRKAteERS 566

                          170       180
                   ....*....|....*....|....*....
gi 1958680058 1048 RLEAWKRA-----EAIENSPKACQYIMAT 1071
Cdd:pfam17380  567 RLEAMEREremmrQIVESEKARAEYEATT 595
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
907-1048 1.24e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 42.59  E-value: 1.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  907 EKVIELESEIEKFKAENTSLAKLRiERESALEKLRKEIADFEQQKARELARIEEYKKEETRKLQKERKVFEKYTAAARTF 986
Cdd:COG1340    140 EKIKELEKELEKAKKALEKNEKLK-ELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEI 218

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958680058  987 PDKKE-----REEIQALKQQIQELQEDLKRKETKwssTHGRLRSQIEMLVKEntdLREEIkvMERFR 1048
Cdd:COG1340    219 VEAQEkadelHEEIIELQKELRELRKELKKLRKK---QRALKREKEKEELEE---KAEEI--FEKLK 277
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 905-1095 1.29e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.83  E-value: 1.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  905 LREKVIELESEIEKFKAENTSLAKLRIERESALEKLRKEIADFEQQKARELARIEEYKKEET---RKLQKERKVFEKYTA 981
Cdd:COG4942     32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAelrAELEAQKEELAELLR 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  982 AA---------------RTFPD----------------------KKEREEIQALKQQIQELQEDLKRKETKWSSTHGRLR 1024
Cdd:COG4942    112 ALyrlgrqpplalllspEDFLDavrrlqylkylaparreqaeelRADLAELAALRAELEAERAELEALLAELEEERAALE 191

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958680058 1025 SQIEMLVKENTDLREEIKVMERFRLEAWKRAEAIENSPKACQYIMATKKDESMNSSIQFQKSHASLGVQGE 1095
Cdd:COG4942    192 ALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKLPWPVSGR 262
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 901-1046 1.41e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 1.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  901 RSQVLREKVIELESEIEKFKAENTSLAKLRIERESALEKLRKEIADFEQQKARELARIEEYKKEETRKLQKERKVFEKYT 980
Cdd:COG1196    672 AALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEE 751

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958680058  981 AAartfPDKKEREEIQALKQQIQELQEDLKR------------KETKwsSTHGRLRSQIEMLVKENTDLREEIKVMER 1046
Cdd:COG1196    752 AL----EELPEPPDLEELERELERLEREIEAlgpvnllaieeyEELE--ERYDFLSEQREDLEEARETLEEAIEEIDR 823
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 901-1055 1.42e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.13  E-value: 1.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  901 RSQVLREKVIELESEIEKFKAENTSLAKLRIEresaLEKLRKEIADFEqqkaRELARIEEYKKEETRKLQKERKVFEKYT 980
Cdd:TIGR02169  362 LKEELEDLRAELEEVDKEFAETRDELKDYREK----LEKLKREINELK----RELDRLQEELQRLSEELADLNAAIAGIE 433

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958680058  981 AAARTFPDKKE--REEIQALKQQIQELQEDLKrketKWSSTHGRLRSQIEMLVKENTDLREEIKvmerfRLEAWKRA 1055
Cdd:TIGR02169  434 AKINELEEEKEdkALEIKKQEWKLEQLAADLS----KYEQELYDLKEEYDRVEKELSKLQRELA-----EAEAQARA 501
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 903-1082 1.57e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 43.03  E-value: 1.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  903 QVLREKVIELESEIEKFKAENTSLAKLRIERESALEKLRKEIADF---------EQQKARELARIEEYKKEETRKL---- 969
Cdd:TIGR00618  552 TSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLqdlteklseAEDMLACEQHALLRKLQPEQDLqdvr 631

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  970 ----QKERKVFEKYTAAAR---TFPDKKEREEIQALKQQIQELQEDLKRKETKWSSTHGRLRSQIEMLVKENTDLREEIK 1042
Cdd:TIGR00618  632 lhlqQCSQELALKLTALHAlqlTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELET 711

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1958680058 1043 VMErfrlEAWKRAEAIENSPKACQYIMAtKKDESMNSSIQ 1082
Cdd:TIGR00618  712 HIE----EYDREFNEIENASSSLGSDLA-AREDALNQSLK 746
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 927-1032 1.77e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.44  E-value: 1.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  927 AKLRIERESALEKLRKEIADFEQQKARElarieeykKEETRKLQKERKVFEKYTAAArtfpdkkeREEIQALKQQIQELQ 1006
Cdd:COG4942     19 ADAAAEAEAELEQLQQEIAELEKELAAL--------KKEEKALLKQLAALERRIAAL--------ARRIRALEQELAALE 82

                           90       100
                   ....*....|....*....|....*.
gi 1958680058 1007 EDLKRKETKWSSTHGRLRSQIEMLVK 1032
Cdd:COG4942     83 AELAELEKEIAELRAELEAQKEELAE 108
FPP pfam05911
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ...
 904-972 2.08e-03

Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.


Pssm-ID: 461778 [Multi-domain]  Cd Length: 859  Bit Score: 42.74  E-value: 2.08e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958680058  904 VLREKVIELESEIEKFKAENTSLAKLRIERESALEKLRKEI----ADFEQQKarelARIEEYKKE------ETRKLQKE 972
Cdd:pfam05911   89 ELEAKLVETEQELLRAAAENDALSRSLQERENLLMKLSEEKsqaeAEIEALK----SRLESCEKEinslkyELHVLSKE 163
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 927-1041 2.17e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 42.38  E-value: 2.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  927 AKLRIERES---ALEKLRKEIADFEQQKARELARIEEYKKEETRKLQKERKVFEKYTAAARtfpdKKEREEiQALKQQIQ 1003
Cdd:COG0542    400 ARVRMEIDSkpeELDELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALK----ARWEAE-KELIEEIQ 474

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1958680058 1004 ELQEDLKRKETKWSSTHGRLRSQIEMLVKENTDLREEI 1041
Cdd:COG0542    475 ELKEELEQRYGKIPELEKELAELEEELAELAPLLREEV 512
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 929-1075 2.36e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.06  E-value: 2.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  929 LRIER-ESALEKLRKEIADFEQQKARELARIEEyKKEETRKLQKERKVFEkytaaartfpdkkerEEIQALKQQIQELQE 1007
Cdd:COG1579     17 SELDRlEHRLKELPAELAELEDELAALEARLEA-AKTELEDLEKEIKRLE---------------LEIEEVEARIKKYEE 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958680058 1008 DLKR----KETKwssthgRLRSQIEMLVKENTDLREEIkvmerfrLEAWKRAEAIENSPKACQYIMATKKDE 1075
Cdd:COG1579     81 QLGNvrnnKEYE------ALQKEIESLKRRISDLEDEI-------LELMERIEELEEELAELEAELAELEAE 139
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
907-1059 2.71e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.06  E-value: 2.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  907 EKVIELESEIEKFKAENTSLAKLriERESALEKLRKEI--------ADFEQQKARELARIEEYKKEETRKLQKERKV--- 975
Cdd:COG4717    337 EELLELLDRIEELQELLREAEEL--EEELQLEELEQEIaallaeagVEDEEELRAALEQAEEYQELKEELEELEEQLeel 414

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  976 FEKYTAAARTFPDKKEREEIQALKQQIQELQEDLKRKETKwsstHGRLRSQIEMLVKENT--DLREEIK-VMERFR--LE 1050
Cdd:COG4717    415 LGELEELLEALDEEELEEELEELEEELEELEEELEELREE----LAELEAELEQLEEDGElaELLQELEeLKAELRelAE 490


                   ....*....
gi 1958680058 1051 AWKRAEAIE 1059
Cdd:COG4717    491 EWAALKLAL 499
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
905-1033 2.89e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.81  E-value: 2.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  905 LREKVIELESEIEKFKAENTSLAKLRIERESALEKLRKEIADFEQQKARELARIEEYKKEETRKLQKERKVFEKYTAAAR 984
Cdd:COG4372     64 LEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQS 143

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958680058  985 TFPDKKerEEIQALKQQIQELQEDLKRKETKWSS-THGRLRSQIEMLVKE 1033
Cdd:COG4372    144 EIAERE--EELKELEEQLESLQEELAALEQELQAlSEAEAEQALDELLKE 191
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 905-1063 2.93e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.93  E-value: 2.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  905 LREKVIELESEIEKFKAENTSLAKLRIERESALEKLRKEIadfeQQKARELARIEEYKKEETRKLQKERKVfekytaaar 984
Cdd:TIGR04523  340 LNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKEN----QSYKQEIKNLESQINDLESKIQNQEKL--------- 406

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958680058  985 tfpDKKEREEIQALKQQIQELQEDLKRketkWSSTHGRLRSQIEMLVKENTDLREEIKVMERFRLEAWKRAEAIENSPK 1063
Cdd:TIGR04523  407 ---NQQKDEQIKKLQQEKELLEKEIER----LKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSIN 478
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
898-1060 4.59e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.56  E-value: 4.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  898 DSVRSQVLREKVIELESEIEKFKAENTslaklriERESALEKLRKEIADFEQQKA-----RE--------LARIEEYKKE 964
Cdd:PRK02224   535 KRERAEELRERAAELEAEAEEKREAAA-------EAEEEAEEAREEVAELNSKLAelkerIEslerirtlLAAIADAEDE 607

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  965 ETRKLQKERKVFEKYTAAARTFPDKKER-------------EEIQALKQQIQELQEDLKRKETKWSSTHGRLRSQIEML- 1030
Cdd:PRK02224   608 IERLREKREALAELNDERRERLAEKRERkreleaefdeariEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVe 687

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1958680058 1031 --VKENTDLREEIKVME--RFRLEA-WKRAEAIEN 1060
Cdd:PRK02224   688 neLEELEELRERREALEnrVEALEAlYDEAEELES 722
CortBP2 pfam09727
Cortactin-binding protein-2; This entry is the first approximately 250 residues of ...
 901-1033 5.39e-03

Cortactin-binding protein-2; This entry is the first approximately 250 residues of cortactin-binding protein 2. In addition to being a positional candidate for autism this protein is expressed at highest levels in the brain in humans. The human protein has six associated ankyrin repeat domains pfam00023 towards the C-terminus which act as protein-protein interaction domains.


Pssm-ID: 462860 [Multi-domain]  Cd Length: 187  Bit Score: 39.51  E-value: 5.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  901 RSQVLREKVIELESEIEKFKAENTSLAKLRIERESALEKLRKEIADFEQQKAR---ELARIEEYKKEETRKLQKERKVFE 977
Cdd:pfam09727   43 GFKYPSDPLLALQRDSELLRDQSQDEDVYEAMYEKPLAELEKLVEKQRETQRRmleQLAAAEKRHRRVIRELEEEKRKHA 122

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958680058  978 KYTAAA--RTFPDKKERE----EIQALKQQIQELQEDLKRKETKWSSTHGRLRSQIEMLVKE 1033
Cdd:pfam09727  123 RDTAQGddFTYLLEKERErlkqELEQEKAQQKRLEKELKKLLEKLEEELSKQKQIALLLVKE 184
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
901-1045 5.54e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.18  E-value: 5.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  901 RSQVLREKVIELESEIEKFKAE-------NTSLAKLRIERESALEKLRKEIADFEQQKARELARIEEYKK------EETR 967
Cdd:PRK02224   280 EVRDLRERLEELEEERDDLLAEaglddadAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREdaddleERAE 359

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958680058  968 KLQKERKVFEKYTAAARTFPDKKeREEIQALKQQIQELQEDLKRKETkwssTHGRLRSQIEMLVKENTDLREEIKVME 1045
Cdd:PRK02224   360 ELREEAAELESELEEAREAVEDR-REEIEELEEEIEELRERFGDAPV----DLGNAEDFLEELREERDELREREAELE 432
PTZ00121 PTZ00121
MAEBL; Provisional
 907-1100 5.67e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 5.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  907 EKVIELESEIEKFKAE--NTSLAKLRIERESALEKLRKEIADFEQQKARELARIEEYKK-EETRKLQKERKVFEkytaAA 983
Cdd:PTZ00121  1233 EEAKKDAEEAKKAEEErnNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKaDEAKKAEEKKKADE----AK 1308

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  984 RTFPDKKEREEIQALKQQIQELQEDLKRKETKWSSTHGRLRSQIEMLVKENTDLREEIKVMERFRLEAWKRAEAI----E 1059
Cdd:PTZ00121  1309 KKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAkkkaE 1388

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1958680058 1060 NSPKACQyimATKKDESMNSSIQFQKSHASLGVQGEKYKKK 1100
Cdd:PTZ00121  1389 EKKKADE---AKKKAEEDKKKADELKKAAAAKKKADEAKKK 1426
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
 905-1013 5.81e-03

Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.


Pssm-ID: 461708 [Multi-domain]  Cd Length: 600  Bit Score: 40.78  E-value: 5.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  905 LREKVIELESEIEKFKAENTSLAKLRIERESALEKLRKEIADFEQQKARELARIEEYKKEET--RKLQK------ERKV- 975
Cdd:pfam05667  340 LQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQYKVKKKTLDLLPDAEEniAKLQAlvdasaQRLVe 419

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958680058  976 ----FEKYTA-----------AARTFPDKKER--EEIQALKQQIQELQEDLKRKE 1013
Cdd:pfam05667  420 lagqWEKHRVplieeyralkeAKSNKEDESQRklEEIKELREKIKEVAEEAKQKE 474
MAT1 pfam06391
CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for ...
 909-1018 5.83e-03

CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for cyclin-dependent kinase-activating kinase (CAK), which interacts with the transcription factor TFIIH. The domain found to the N-terminal side of this domain is a C3HC4 RING finger.


Pssm-ID: 461894 [Multi-domain]  Cd Length: 202  Bit Score: 39.53  E-value: 5.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  909 VIELESEIEKFKAENTSLAKLRIERESA----LEKLRKEIADFEQQKARELARIEEYKKEETRKLQKE------------ 972
Cdd:pfam06391   63 VEETEKKIEQYEKENKDLILKNKMKLSQeeeeLEELLELEKREKEERRKEEKQEEEEEKEKKEKAKQElidelmtsnkda 142

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1958680058  973 RKVFEKYTAAARtfpdKKEREEiqalKQQIQELQEDLKRKETKWSS 1018
Cdd:pfam06391  143 EEIIAQHKKTAK----KRKSER----RRKLEELNRVLEQKPTQFST 180
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 903-1064 6.08e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.58  E-value: 6.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  903 QVLREKVIELESEIEKFKAE----NTSLAKLRIERESALEKLRKEIADFEQQKARE---------------------LAR 957
Cdd:COG3883     47 EELNEEYNELQAELEALQAEidklQAEIAEAEAEIEERREELGERARALYRSGGSVsyldvllgsesfsdfldrlsaLSK 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  958 IEEYKKEETRKLQKERKVFEKYTAAARtfpdkKEREEIQALKQQIQELQEDLKRKETKWSSTHGRLRSQIEMLVKENTDL 1037
Cdd:COG3883    127 IADADADLLEELKADKAELEAKKAELE-----AKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAEL 201

                          170       180
                   ....*....|....*....|....*..
gi 1958680058 1038 REEIKVMERFRLEAWKRAEAIENSPKA 1064
Cdd:COG3883    202 EAELAAAEAAAAAAAAAAAAAAAAAAA 228
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 905-1041 6.15e-03

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 40.43  E-value: 6.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  905 LREKVIELESEIEKFKAENTSlaklrieRESALEKLRKEIADF--EQQKARELARIEEYKKEetrkLQKERKvfeKYTAA 982
Cdd:cd22656    133 YQDKAAKVVDKLTDFENQTEK-------DQTALETLEKALKDLltDEGGAIARKEIKDLQKE----LEKLNE---EYAAK 198

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958680058  983 ARtfpdkkerEEIQALKQQIQELQEDLKRKEtkwssthgRLRSQIEMLVKENTDLREEI 1041
Cdd:cd22656    199 LK--------AKIDELKALIADDEAKLAAAL--------RLIADLTAADTDLDNLLALI 241
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 903-1064 7.08e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.52  E-value: 7.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  903 QVLREKVIELESEIEKFKAENTSLaklrierESALEKLRKEIAD-----------------FEQQKARELAR-------I 958
Cdd:COG4942     72 RALEQELAALEAELAELEKEIAEL-------RAELEAQKEELAEllralyrlgrqpplallLSPEDFLDAVRrlqylkyL 144

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  959 EEYKKEETRKLQKERKVFEKYTAAArtfpdKKEREEIQALKQQIQELQEDLKRKETKWSSTHGRLRSQIEMLVKENTDLR 1038
Cdd:COG4942    145 APARREQAEELRADLAELAALRAEL-----EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQ 219

                          170       180
                   ....*....|....*....|....*.
gi 1958680058 1039 EEIKVMERFRLEAWKRAEAIENSPKA 1064
Cdd:COG4942    220 QEAEELEALIARLEAEAAAAAERTPA 245
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
887-1014 8.06e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.39  E-value: 8.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680058  887 KLSLSQDQPP--GDSVRSQVLREKVIELESEIEKFKAENTslaklriERESALEKLRKEIADFEQQKARELARIEEYKKE 964
Cdd:COG3206    248 QLGSGPDALPelLQSPVIQQLRAQLAELEAELAELSARYT-------PNHPDVIALRAQIAALRAQLQQEAQRILASLEA 320

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958680058  965 ETRKLQKERKVFEKYTAAArtfpdKKEREEIQALKQQIQELQEDLKRKET 1014
Cdd:COG3206    321 ELEALQAREASLQAQLAQL-----EARLAELPELEAELRRLEREVEVARE 365
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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